Binding of bisubstrate analog promotes large structural changes in the unregulated catalytic trimer of aspartate transcarbamoylase: Implications for allosteric regulation

Lignende værker

• Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit
  af: Beernink, Peter T., et al.
  Udgivet: (1999)
• Charge neutralization in the active site of the catalytic trimer of aspartate transcarbamoylase promotes diverse structural changes
  af: Endrizzi, James A., et al.
  Udgivet: (2017)
• Reconstitution of active catalytic trimer of aspartate transcarbamoylase from proteolytically cleaved polypeptide chains.
  af: Powers, V. M., et al.
  Udgivet: (1993)
• In vivo formation of allosteric aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains: implications for protein folding and assembly.
  af: Zhang, P., et al.
  Udgivet: (1996)
• Pathways of Assembly of Aspartate Transcarbamoylase from Catalytic and Regulatory Subunits
  af: Bothwell, M., et al.
  Udgivet: (1974)